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• W2034160988 abstract "Based on the interpretation of X-ray diffraction data reported for crystals of the poly-l-glutamine-rich 19-peptide D2Q15K2, Perutz et al. (Proc. Natl. Acad. Sci. USA 2002, 99, 5591−5595) proposed that hollow, water-filled nanotubes are the basic structural motif of amyloid fibers. We are able to offer an alternative interpretation for the same X-ray diffraction data. Our proposed structure consists of β-sheets, limited in size in the chain direction that stack at an intersheet distance of 0.83 nm to form cross-β crystallites. The β-sheets are composed of individual D2Q15K2 molecules hydrogen bonding together in the a direction. The relatively linear interchain amide hydrogen bonds in this growth direction occur at two sites: (i) between neighboring backbone amides and (ii) between adjacent (glutamine) side chain amides decorating both surfaces of the β sheet. The polyQ sub-lattice unit cell is orthorhombic with parameters a =0.950 nm, b = 1.660 nm, and c = 0.695 nm; contains two β-sheet segments; and has a calculated density of 1.54 g cm-3. A key ingredient in the proposed structure is the locking of the Q side chains by hydrogen bonding, which allow high-density packing. In addition, there is evidence suggesting that the D2Q15K2 molecules adopt a once-folded hairpin conformation." @default.
• W2034160988 created "2016-06-24" @default.
• W2034160988 creator A5044232169 @default.
• W2034160988 creator A5048313857 @default.
• W2034160988 date "2004-12-04" @default.
• W2034160988 modified "2023-10-16" @default.
• W2034160988 title "New Model for Crystalline Polyglutamine Assemblies and Their Connection with Amyloid Fibrils" @default.
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• W2034160988 doi "https://doi.org/10.1021/bm0494388" @default.
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